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The self-assembly of lipopeptides containing short peptide fragments derived from the gastrointestinal hormone PYY3-36: from micelles to amyloid fibrils

DOI: 10.1021/acs.jpcb.8b11097 DOI Help

Authors: Jessica A. Hutchinson (University of Reading) , Ian W. Hamley (University of Reading) , Juan Torras (Universitat Politècnica de Catalunya) , Carlos Alemán (Universitat Politècnica de Catalunya) , Dr Jani Seitsonen (Aalto University) , Janne Ruokolainen (Aalto University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Journal Of Physical Chemistry B

State: Published (Approved)
Published: January 2019
Diamond Proposal Number(s): 19477

Abstract: We investigate the impact of lipidation on the self-assembly of two peptide fragments from the gastrointestinal peptide hormone PYY3-36. The lipopeptides C16IKPEAP and C16IKPEAPGE contain the first 6 and 8 amino acid residues respectively from the PYY3-36 peptide sequence, with a palmitoyl C16 tail attached at the N-terminus. These lipopeptides form spherical micelles in aqueous solution, above a critical micelle concentration (cmc), which is pH-dependent. Modelling of small-angle x-ray scattering data along with molecular dynamics simulations shows the formation of micelles with a hydrophobic interior and a well hydrated exterior. The lipopeptides have a disordered conformation over the pH and temperature range studied. The cmc is found to be independent of temperature, pointing to athermal micellization. In contrast to the presence of hydrated micelles in solution, β-sheet amyloid fibrils form in dried samples. Thus, the nanostructure of lipidated PYY3-36 fragment peptides can be tuned by control of pH or concentration, for future applications.

Subject Areas: Chemistry


Beamlines: B21-High Throughput SAXS